HUMAN RECOMBINANT ANTI-MULLERIAN HORMONE: A SELF-ACTIVATING DRUG
- 作者: Rak A.1,2, Trofimov A.1, Ischenko A.1
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隶属关系:
- State Research Institute for Highly Pure Biopreparations
- Saint-Petersburg State University
- 期: 卷 22, 编号 2-1 (2019)
- 页面: 486-488
- 栏目: ORIGINAL ARTICLES
- URL: https://journals.rcsi.science/1028-7221/article/view/120276
- DOI: https://doi.org/10.31857/S102872210006939-7
- ID: 120276
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详细
Here, the autoproteolytic activity of human recombinant anti-Mullerian hormone (rAMH), a potential antineoplastic drug, was investigated. It was shown that the hormone is not only able to activate itself by the limited proteolysis, but also specifically interacts with the proteolytic inhibitor aprotinin. The involvement of the rAMH specific proteolysis site in interaction with a specifi c receptor type II (MISRII) was found. The data obtained may be useful to clarify some aspects of the native AMH biochemistry and pharmacodynamics of the recombinant hormone.
作者简介
A. Rak
State Research Institute for Highly Pure Biopreparations;Saint-Petersburg State University
编辑信件的主要联系方式.
Email: a.ya.rak@hpb.spb.ru
Junior Researcher of the Protein Biochemistry Laboratory;
PhD student,
St. Petersburg
俄罗斯联邦A. Trofimov
State Research Institute for Highly Pure Biopreparations
Email: fake@neicon.ru
Group Head of the Protein Biochemistry Laboratory,
St. Petersburg
俄罗斯联邦A. Ischenko
State Research Institute for Highly Pure Biopreparations
Email: fake@neicon.ru
PhD, Head of the Protein Biochemistry Laboratory,
St. Petersburg
俄罗斯联邦参考
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- Rak A. Ya., Trofi mov A. V., Protasov E. A., Rodin S. V., Zhakhov A. V., Zabrodskaya Ya. A., Ischenko A. M. Spontaneous proteolytic processing of human recombinant anti-mullerian hormone: structural and functional differences of the molecular forms. Appl Biochem Microbiol. 2019, 55(1),13–20.
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